Journal Article PreJuSER-5102

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png
Solution structure of the Mesorhizobium loti K1 channel cyclic nucleotide-binding domain in complex with cAMP

 ;  ;  ;  ;

2009
Nature Publishing Group London [u.a.]

EMBO reports 10, 729 - 735 () [10.1038/embor.2009.68]

This record in other databases:    

Please use a persistent id in citations: doi:

Abstract: Cyclic nucleotide-sensitive ion channels, known as HCN and CNG channels, are crucial in neuronal excitability and signal transduction of sensory cells. HCN and CNG channels are activated by binding of cyclic nucleotides to their intracellular cyclic nucleotide-binding domain (CNBD). However, the mechanism by which the binding of cyclic nucleotides opens these channels is not well understood. Here, we report the solution structure of the isolated CNBD of a cyclic nucleotide-sensitive K(+) channel from Mesorhizobium loti. The protein consists of a wide anti-parallel beta-roll topped by a helical bundle comprising five alpha-helices and a short 3(10)-helix. In contrast to the dimeric arrangement ('dimer-of-dimers') in the crystal structure, the solution structure clearly shows a monomeric fold. The monomeric structure of the CNBD supports the hypothesis that the CNBDs transmit the binding signal to the channel pore independently of each other.

Keyword(s): Alphaproteobacteria: chemistry (MeSH) ; Crystallography, X-Ray (MeSH) ; Cyclic AMP: chemistry (MeSH) ; Cyclic AMP: metabolism (MeSH) ; Cyclic Nucleotide-Gated Cation Channels: chemistry (MeSH) ; Cyclic Nucleotide-Gated Cation Channels: metabolism (MeSH) ; Models, Molecular (MeSH) ; Potassium Channels: chemistry (MeSH) ; Potassium Channels: metabolism (MeSH) ; Protein Structure, Secondary (MeSH) ; Protein Structure, Tertiary (MeSH) ; Solutions (MeSH) ; Cyclic Nucleotide-Gated Cation Channels ; Potassium Channels ; Solutions ; Cyclic AMP ; J ; NMR solution structure (auto) ; MloK1 (auto) ; ion channels (auto) ; HCN (auto) ; CNG (auto)


Note: This study was supported by a research grant from the Helmholtzgemeinschaft

Contributing Institute(s):
  1. Zelluläre Biophysik (ISB-1)
  2. Strukturbiochemie (ISB-3)
  3. Jülich Aachen Research Alliance - High-Performance Computing (JARA-HPC)
Research Program(s):
  1. Programm Biosoft (N03)
  2. Funktion und Dysfunktion des Nervensystems (P33)

Appears in the scientific report 2009
Click to display QR Code for this record

The record appears in these collections:
Document types > Articles > Journal Article
JARA > JARA > JARA-JARA\-HPC
Institute Collections > IBI > IBI-7
Institute Collections > IBI > IBI-1
Workflow collections > Public records
ICS > ICS-4
ICS > ICS-6
Publications database

 Record created 2012-11-13, last modified 2020-04-23


Restricted:
Download fulltext PDF
External link:
Download fulltextFulltext by Pubmed Central
Rate this document:

Rate this document:
1
2
3
 
(Not yet reviewed)